F5152
D-Fructose Dehydrogenase from Gluconobacter industrius
lyophilized powder, 400-1,200 units/mg protein
别名:
D-Fructose:(acceptor) 5-oxidoreductase
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
400-1,200 units/mg protein
form
lyophilized powder
Quality Level
specific activity
400-1,200 units/mg protein
mol wt
140 kDa
composition
Protein, ≤10% Lowry
shipped in
wet ice
storage temp.
−20°C
Application
D-fructose dehydrogenase is used as a biosensor to detect the presence of D-fructose.
Fructose dehydrogenase (FDH) is used in a number of basic research projects to examine the electrochemical properties of enzyme-catalyzed electrode reactions called bioelectrocatalysis. D-fructose dehydrogenase has been used in a study that contributed towards a convenient method for measuring rare sugars, monosaccharides, for applications in the bio-industry. A direct electron transfer reaction of d-fructose dehydrogenase adsorbed on a porous carbon electrode surface has been used to describe a batch-type coulometric d-fructose biosensor.
Biochem/physiol Actions
D-fructose dehydrogenase catalyzes the oxidation of D-fructose to 5-keto-D-fructose.
Fructose dehydrogenase (FDH) is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively.
Physical form
Lyophilized powder containing citrate-phosphate buffer salts, TRITON® X-100, and stabilizer
Other Notes
One unit will convert 1.0 μmole D-fructose to 5-ketofructose per min at pH 4.5 at 37 °C.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
Seiya Tsujimura et al.
Analytical chemistry, 81(22), 9383-9387 (2009-11-17)
This paper describes a batch-type coulometric d-fructose biosensor based on direct electron transfer reaction of d-fructose dehydrogenase (FDH) adsorbed on a porous carbon electrode surface. The adsorbed-FDH electrodes catalyzed the electrochemical two-electron oxidation of d-fructose to 5-keto-d-fructose without a mediator.
Ana Dominguez et al.
Revista iberoamericana de micologia, 23(3), 189-191 (2007-01-02)
Several microorganisms are reported to have transfructosylation activity due to fructosyltransferase and/or fructofuranosidase activities. However, the search for other fungi with higher transfructosylation activity remains a challenge. So, a presumptive and indirect colorimetric plate assay for the evaluation of transfructosylation
Takeo Miyake et al.
Journal of the American Chemical Society, 133(13), 5129-5134 (2011-03-12)
Nanostructured carbons have been widely used for fabricating enzyme-modified electrodes due to their large specific surface area. However, because they are random aggregates of particular or tubular nanocarbons, the postmodification of enzymes to their intrananospace is generally hard to control.
Yuko Sasaki et al.
Analytical biochemistry, 417(1), 129-135 (2011-06-29)
The catalytic activity of a membrane-bound enzyme, d-fructose dehydrogenase (FDH), at the polarized oil/water (O/W) interface was studied. Multisweep cyclic voltammetry and ac voltammetry were carried out to show the irreversible adsorption of FDH at the interface. Using the thusly
Determination of seminal fructose using D-fructose dehydrogenase.
K Nakashima et al.
Clinica chimica acta; international journal of clinical chemistry, 151(3), 307-310 (1985-10-15)
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